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Identification test Content analysis Toxicity Usage limitation Chemical Properties Usage Production
L-Serine structure
Chemical Name:
Molecular Formula:
Formula Weight:
MOL File:

L-Serine Properties

Melting point:
222 °C (dec.) (lit.)
15.2 º (c=10, 2N HCl)
Boiling point:
197.09°C (rough estimate)
refractive index 
1.4368 (estimate)
Flash point:
storage temp. 
H2O: 50 mg/mL
2.19(at 25℃)
5-6 (100g/l, H2O, 20℃)
optical activity
[α]20/D +13.5±0.5°, c = 5% in 5 M HCl
Water Solubility 
250 g/L (20 ºC)
λ: 260 nm Amax: 0.05
λ: 280 nm Amax: 0.05
150 ºC
Stable. Incompatible with strong oxidizing agents.
CAS DataBase Reference
56-45-1(CAS DataBase Reference)
Substances Added to Food (formerly EAFUS)
EWG's Food Scores
NIST Chemistry Reference
EPA Substance Registry System
L-Serine (56-45-1)
  • Risk and Safety Statements
Hazard Codes  Xi
Risk Statements  36/37/38
Safety Statements  24/25-36-26
WGK Germany  3
RTECS  VT8100000
HS Code  29225000

L-Serine price More Price(37)

Manufacturer Product number Product description CAS number Packaging Price Updated Buy
Sigma-Aldrich 8.16020 (S)-(+)-Serine for synthesis 56-45-1 25 g $34.78 2021-03-22 Buy
Sigma-Aldrich 5650 L-Serine - CAS 56-45-1 - Calbiochem 56-45-1 100 g $77.61 2021-03-22 Buy
Sigma-Aldrich 8.16020 (S)-(+)-Serine for synthesis 56-45-1 100 g $94.35 2021-03-22 Buy
Sigma-Aldrich 54763 L-Serine certified reference material, TraceCERT 56-45-1 100mg $104 2021-03-22 Buy
Sigma-Aldrich 1612506 L-Serine United States Pharmacopeia (USP) Reference Standard 56-45-1 200mg $429 2021-03-22 Buy

L-Serine Chemical Properties,Uses,Production

Identification test

1ml ninhydrin (TS-250) was added to 5ml sample solution (0.1%) should produce red purple or violet color. 200mg Periodic acid was added to the above solution and heated. Dissolving a sample of about 500 rag in 10 ml water, adding 200 mg of Periodic acid and heating, should produce the smell of formaldehyde.

Content analysis

Same as "DL-serine (01126)"


It can be used in food safely (FDA,§172.320,2000).

Usage limitation

It takes up to 8.4% of total protein quantity(FDA,§172.320,2000).

Chemical Properties

Six-sided flaky crystal or prismatic crystal, soluble in water(20℃,25g/100ml water)


Used as a biochemical reagent and food additive, Used for biochemical research, the preparation of tissue culture, and used as amino acids nutrition medicine.


L-Serine can be obtained by a variety of methods. Methods common seen are as follows:
1. Obtain it though the hydrolysis of protein with a high content of L – Serine and recycled by ion exchange resin;
2. Obtain it by the reaction between ethyl formate and ethylhippurate;
3. Obtain it by using carbohydrate as the starting material through zymotechnics;
4. In alkaline condition, the raw material of  DL-serine and chloracetyl chloride reacted, then, extracted with ethyl acetate after drying by distillation, treated by active carbon, chiral separated by acylation enzyme to obtain the product;
5. Hydrolysis:
The raw material of silkworm cocoon was hydrolyzed in acid condition and separated and purified with ion exchange water. process engineering: silkworm cocoon [acid hydrolysis]→[HCl, 110℃, 24h] hydrolysate [deacidification,decoloration]→[732resin,ammonia,pH3.5-8] eluant [fractionation]→[717 resin] drips [Concentration, crystallization, and refined]→[film evaporation]→L-serine
Acid hydrolysis: Adding 30 kg silkworm cocoon to a crock, then adding 150 L HCl With a concentration of 6 mol/L, stirting heating to 110 ℃ for 24 h, after cooling below 60 ℃, filtering and washing the filter residue with pure water of five times the amount of filtrate, at five times the filtrate volume of washing, merging the  washing liquor into the filtrate to obtain 800 L of aqueous solution.
Deacidification and liquid-removal: 100L of hydrolysate flows through H + type 732 cation exchange resin column (150 mm x 2000 mm polyvinyl chloride, filled with 25L resin for each of the 2 columns) from top to bottom with a flow velocity of 100-120ml/min,
, then washed with purified water to remove pigments to obtain clear liquid without Cl-.0.3 mol/L ammonia flows through the column from top to bottom with a flow velocity of 80-100ml/min till outflow of amino acids, collecting the eluent within pH3.5-8. Finally, 1 mol/L of ammonia was used to wash Tyrosine followed by deammoniation, concentration and crystallization to obtain crude tyrosine.
The above eluent was separated with 4 regular OH-type 717 Anion exchange resin columns:
Column1 50mm×2000mm, filled with 24L resin (polyvinyl chloride)
Column2 150mm×1800mm, filled with 22L resin (polyvinyl chloride)
Column3 150mm×1600mm, filled with 20L resin (polyvinyl chloride)
Column4 150mm×1400mm, filled with 10L resin (polyvinyl chloride)
Firstly, the pH value of the eluent was adjusted to 7-8 with 1mol/L NaOH Solution. Then, the eluent was separated in the first column with the flow rate of 120-150 ml/min until the saturation of the resin and washed to neutral with pure water. Column1 and column2 were connected in series, eluted using 0.1 mol/L HCl with the flow rate of 80-100 ml/min, collected 25 reagent Bottles ((1000 ml/bottle)until the appearance of amino acid in effluent. Colunm 4 was then connected in series and the elution process was continued. About 50 reagent Bottles were collected until the appearance of amino acid in effluent and the pH value of the eluent reached 2-3.
Paper chromatography was used to purify and collect extracts containing serine.
After concentration, crystallization, and refinement, the above extraction was evaporated and concentrated until crystallization occurrence. After cooling, anhydrous ethanol which is 2 times the amount of the extraction was added, stored in a refrigerator overnight, and dried after crystal precipitation to obtain L-Serine. The yield is about 4% Calculated on cocoon.
6. Hydrolysis:
Fermentation with precursor addition
The in vivo metabolism speed of L-Serine is very fast and direct fermentation production is difficult.  Generally, the method of fermentation with precursor addition is adopted. The precursors mainly include glycine, betaine and glyceric acid, among which Fermentation with glyceric acid precursor has been industrialized. Producing strains include anaerobic type and Methylotrophs.
Heterotroph, glycine produced L-Serin
glycine [Glycine rod acid , Butane Nocardia or white sarcina]→[fermentation] L-Serine.
Methylotrophs   glycine produced L-Serin
glycine[pseudomonas, Hyphomicrobium or Methanol assimilation Arthrobacter globiformis] →[fermentation] L-Serine.
7. Chemical synthesis:
DL-Serine can be synthesized by using glycolaldehyde as raw material and
and chiral separated to obtain L-Serine.
Synthesis by using glycolaldehyde as raw material
Synthesis by using diethyl bromomalonate as raw material
Synthesis by using Vinyl compounds as raw material
8. Enzymatic method:
Chemically synthesized DL-2 Oxazolidine-4-carboxylic acid (DL-OOC)
was used as raw material to produce L – serine under the catalysis of
testosterone pseudomonas produced L-OOC hydrolase or Bacillus subtilis
produced OOC racemase.
DL-2-Oxazolidine-4-carboxylic acid (DL-OOC)[L-OOC hydrolase or racemase]→L-serine


Serine (abbreviated as Ser or S) is an amino acid with the formula HO2CCH(NH2)CH2OH. It is one of the proteinogenic amino acids. Its codons in the genetic code are UCU, UCC, UCA, UCG, AGU and AGC. By virtue of the hydroxyl group, serine is classified as a polar amino acid.

Chemical Properties

White crystalline powder


Amino acid.


ChEBI: The L-enantiomer of serine.

Production Methods

Industrially , L - serine is produced by fermentation, with an estimated 100 - 1000 tonnes per year produced . In the laboratory, racemic serine can be prepared from methyl acrylate via several steps.

Biotechnological Production

Serine is the first amino acid produced in the 3-phosphoglycerate pathway. It is further converted to glycine and L-cysteine. Industrially L-serine can be produced by direct fermentation or by an enzymatic process from glycine. The enzymatic route developed by Mitsui reacts glycine with formaldehyde using serine hydroxymethyltransferase (SHMT). With an overexpression of SHMT in E. coli, concentrations of serine of over 300 g/L in 35 h reaction time have been reported, with a glycine conversion of[98 %. This process requires the addition of tetrahydrofolic acid to the system as a cofactor. An alternative to enzymatic production is a direct fermentation to give L-serine. Strains based on Brevibacterium flavum and C. glutamicum have been described. In both strains, the enzymes phosphoglycerate dehydrogenase (serA), phosphoserine phosphatase (serB), and phosphoserine transaminase (serC) have been overexpressed. These enzymes are involved in the biosynthesis pathway from 3-phosphoglycerate. Note that because of product inhibition by L-serine of serA, feedback-resistant mutants have been developed to increase yields. A mutant strain of B. flavum with a feedback-resistant serA* and overexpression of the serA*, serB, and serC has been reported to accumulate 35.2 g/L L-serine with a carbon yield of 32 % based on glucose. In addition it has been shown that increased yields in C. glutamicum can be obtained by deleting the L-serine degrading enzyme L-serine dehydratase (sdaA).

Biological Activity

Endogenous agonist at the inhibitory glycine receptor.

Biotechnological Applications

Serine is important in metabolism in that it participates in the biosynthesis of purines and pyrimidines. It is the precursor to several amino acids including glycine and cysteine, and tryptophan in bacteria. It is also the precursor to numerous other metabolites, including sphingolipids and folate, which is the principal donor of one-carbon fragments in biosynthesis.
Structural role
Serine plays an important role in the catalytic function of many enzymes. It has been shown to occur in the active sites of chymotrypsin, trypsin, and many other enzymes. The so-called nerve gases and many substances used in insecticides have been shown to act by combining with a residue of serine in the active site of acetylcholine esterase, inhibiting the enzyme completely.
As a constituent (residue) of proteins, its side chain can undergo O-linked glycosylation, which may be functionally related to diabetes.
It is one of three amino acid residues that are commonly phosphorylated by kinases during cell signaling in eukaryotes. Phosphorylated serine residues are often referred to as phosphoserine.
D-Serine, synthesized in the brain by serine racemase from Lserine (its enantiomer), serves as both a neuro transmitter and a gliotransmitter by coactivating NMDA receptors, making them able to open if they then also bind glutamate. D-serine is a potent agonist at the glycine site of the NMDA-type glutamate receptor. For the receptor to open, glutamate and either glycine or D-serine must bind to it. In fact, D-serine is a more potent agonist at the glycine site on the NMDAR than glycine itself. D-serine was only thought to exist in bacteria until relatively recently; it was the second D amino acid discovered to naturally exist in humans, present as a signalling molecule in the brain, soon after the discovery of D-aspartate. Had D amino acids been discovered in humans sooner, the glycine site on the NMDA receptor might instead be named the D-serine site.
Gustatory sensation
Pure D-Serine is an off-white crystalline powder with a very faint funky or dirty aroma. L-Serine is sweet with minor umami and sour tastes at high concentration. D-Serine is sweet with an additional minor sour taste at medium and high concentrations.

Chemical Synthesis

This compound is one of the naturally occurring proteinogenic amino acids. Only the L-stereoisomer appears naturally in proteins. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865. Its name is derived from the Latin for silk, sericum. Serine's structure was established in 1902.
The biosynthesis of serine starts with the oxidation of 3- phosphoglycerate to 3-phosphohydroxypyruvate and NADH. Reductive amination of this ketone followed by hydrolysis gives serine. Serine hydroxymethyltransferase catalyzes the reversible, simultaneous conversions of L-serine to glycine (retro-aldol cleavage) and 5,6,7,8-tetra hydrofolate to 5,10-methylene tetra hydrofolate (hydrolysis).
This compound may also be naturally produced when UV light illuminates simple ices such as a combination of water, methanol, hydrogen cyanide, and ammonia, suggesting that it may be easily produced in cold regions of space.

Purification Methods

A likely impurity is glycine. Crystallise L-serine from H2O by adding 4volumes of EtOH. Dry and store it in a desiccator. It sublimes at 160-170o/0.3mm with 99.7% recovery, and unracemised [Gross & Gradsky J Am

L-Serine Preparation Products And Raw materials

Raw materials

Preparation Products

L-Serine Suppliers

Global( 630)Suppliers
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Capot Chemical Co.,Ltd.
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+86-571-85864795 China 20010 60
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+86-371-66670886 China 21031 58
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Hefei TNJ Chemical Industry Co.,Ltd.
86-0551-65418684 18949823763
86-0551-65418684 China 3001 55
Shanghai Zheyan Biotech Co., Ltd.
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View Lastest Price from L-Serine manufacturers

Image Release date Product Price Min. Order Purity Supply Ability Manufacturer
2021-10-19 L-Serine
US $48.00-40.00 / KG 1KG 99% 200tons Guangzhou Sunton Biotechnology Co., Ltd.
2021-09-29 L-Serine
US $0.00 / Kg/Drum 1KG 98.5%-101.5% 10 TONS WUHAN FORTUNA CHEMICAL CO., LTD
2021-08-26 L-Serine
US $40.00 / KG 1KG 99% 5000kg Hebei Crovell Biotech Co Ltd

L-Serine Spectrum

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